Elucidating the interaction mechanism of rutin with β-casein and β-lactoglobulin: A comprehensive analysis using multi-spectroscopy, molecular docking, and molecular dynamic simulations.

• Tác giả: Wentao Chen, Yu Fang, Guoqiang Li, Peng Li, Shufen Lin, Xinyan Lin, Hailin Wang, Leiwen Xiang, Zhuangwei Zhang
• Ngôn ngữ: eng
• Ký hiệu phân loại: 577.51 Coastal ecology
• Thông tin xuất bản: England : Food chemistry , 2025
• Bộ sưu tập: NCBI
• ID: 643410

Tóm tắt

 Polyphenol-protein interactions are crucial for food processing, nutrition, and functional properties. This study investigates the interaction between rutin and β-casein (β-CAS) or β-lactoglobulin (β-LG) using multispectral analysis, molecular docking, and molecular dynamics (MD) simulations. Fluorescence spectroscopy reveals that rutin binds spontaneously (ΔG <
  0) to β-CAS and β-LG, forming complexes with binding constants (Ka) at 298 K of 42.500 × 10